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Conserved domains on  [gi|1054581693|ref|WP_066350436|]
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UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase [Aliarcobacter skirrowii]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
5-374 3.41e-164

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member TIGR03588:

Pssm-ID: 450240  Cd Length: 380  Bit Score: 464.49  E-value: 3.41e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   5 IPYGKQSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFV 83
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALgVGPGDRVWTTPITFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  84 ATSNSILYVEAIPIFVDIQ-EDGNIDLDLCEEELKKDSS--IKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLG 160
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDpDTGNIDEDALEKKLAAAKGklPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 161 ASFGNIKAGSCENSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKR------FPDTAPWYYEMHSLGFNY 234
Cdd:TIGR03588 161 AEYGGKPVGNCRYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKdpllfeKQDEGPWYYEQQELGFNY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 235 RITDMQVALGISQLKKLDSFIKRRKEIALKYDKAFL-NSFVKPLYSFTNN-SSYHLFVVKVDFsKLNISKIELFNKMREK 312
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKdLPYFTPLTIPLGSkSAWHLYPILLDQ-EFGCTRKEVFEALRAA 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054581693 313 NIGLQLHYIPINKQPYYKYlGYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
 
Name Accession Description Interval E-value
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
5-374 3.41e-164

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 464.49  E-value: 3.41e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   5 IPYGKQSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFV 83
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALgVGPGDRVWTTPITFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  84 ATSNSILYVEAIPIFVDIQ-EDGNIDLDLCEEELKKDSS--IKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLG 160
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDpDTGNIDEDALEKKLAAAKGklPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 161 ASFGNIKAGSCENSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKR------FPDTAPWYYEMHSLGFNY 234
Cdd:TIGR03588 161 AEYGGKPVGNCRYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKdpllfeKQDEGPWYYEQQELGFNY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 235 RITDMQVALGISQLKKLDSFIKRRKEIALKYDKAFL-NSFVKPLYSFTNN-SSYHLFVVKVDFsKLNISKIELFNKMREK 312
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKdLPYFTPLTIPLGSkSAWHLYPILLDQ-EFGCTRKEVFEALRAA 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054581693 313 NIGLQLHYIPINKQPYYKYlGYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-374 2.53e-152

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 433.73  E-value: 2.53e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   4 FIPYGKQSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSF 82
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALgIGPGDEVITPAFTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  83 VATSNSILYVEAIPIFVDIQED-GNIDLDLCEEELKKDssIKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGA 161
Cdd:COG0399    81 VATANAILYVGATPVFVDIDPDtYNIDPEALEAAITPR--TKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 162 SFGNIKAGSCenSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKRFPDtapwyYEMHSLGFNYRITDMQV 241
Cdd:COG0399   159 TYKGKKVGTF--GDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAK-----YEHVELGYNYRMDELQA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 242 ALGISQLKKLDSFIKRRKEIALKYDKAF--LNSFVKPLYSFTNNSSYHLFVVKVDfskLNISKIELFNKMREKNIGLQLH 319
Cdd:COG0399   232 AIGLAQLKRLDEFIARRRAIAARYREALadLPGLTLPKVPPGAEHVYHLYVIRLD---EGEDRDELIAALKARGIGTRVH 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054581693 320 Y-IPINKQPYYKYLGYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:COG0399   309 YpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
16-370 5.05e-131

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 379.19  E-value: 5.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  16 DINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFVATSNSILYVEA 94
Cdd:cd00616     1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALgIGPGDEVIVPSFTFVATANAILLLGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  95 IPIFVDIQED-GNIDLDLCEEELKKDssIKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGASFGNIKAGSCen 173
Cdd:cd00616    81 TPVFVDIDPDtYNIDPELIEAAITPR--TKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTF-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 174 SDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKRFpdtaPWYYEMHSLGFNYRITDMQVALGISQLKKLDS 253
Cdd:cd00616   157 GDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRD----RFKYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 254 FIKRRKEIALKYDKAFLN-SFVKPLYSFTNN-SSYHLFVVKVDfSKLNISKIELFNKMREKNIGLQLHYIPIN-KQPYYK 330
Cdd:cd00616   233 IIARRREIAERYKELLADlPGIRLPDVPPGVkHSYHLYVIRLD-PEAGESRDELIEALKEAGIETRVHYPPLHhQPPYKK 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1054581693 331 YLGYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTL 370
Cdd:cd00616   312 LLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
10-371 4.53e-118

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 346.58  E-value: 4.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  10 QSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFVATSNS 88
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALgVGPGDEVITPSFTFVATANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  89 ILYVEAIPIFVDIQ-EDGNIDLDLCEEELKKDSsiKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGASFGNIK 167
Cdd:pfam01041  81 ALRLGAKPVFVDIDpDTYNIDPEAIEAAITPRT--KAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 168 AGSCenSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKRfPDTAPWYYEMhsLGFNYRITDMQVALGISQ 247
Cdd:pfam01041 159 VGTL--GDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVR-KADKRYWHEV--LGYNYRMTEIQAAIGLAQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 248 LKKLDSFIKRRKEIALKYDKAFL---NSFVKPLYSFTNNSSYHLFVVKVDFSKlnISKIELFNKMREKNIGLQLHY-IPI 323
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLAdlpGFTPLTTPPEADVHAWHLFPILVPEEA--INRDELVEALKEAGIGTRVHYpIPL 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1054581693 324 NKQPYYKYL-GYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTLF 371
Cdd:pfam01041 312 HLQPYYRDLfGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
1-374 4.05e-65

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 211.42  E-value: 4.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   1 MIDFIPYGKQSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTP 79
Cdd:PRK11658    1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALgIGPGDEVITPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  80 NSFVATSNSILYVEAIPIFVDIQEDG-NIDLDLCEEELKkdSSIKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHS 158
Cdd:PRK11658   81 LTWVSTLNMIVLLGATPVMVDVDRDTlMVTPEAIEAAIT--PRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 159 LGASFGNIKAGScenSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIK----------RFPDTapwyyEMH 228
Cdd:PRK11658  159 VGTYYKGRHIGA---RGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGvdafdrqtqgRAPQA-----EVL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 229 SLGFNYRITDMQVALGISQLKKLDSFIKRRKEIALKYDKAFLNSFVKPLY--SFTNNSSYHLFVVKVDFSKLNISKIELF 306
Cdd:PRK11658  231 TPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSlpAWPHQHAWHLFIIRVDEERCGISRDALM 310
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054581693 307 NKMREKNIGLQLHYIPINKQPYYKylgygnEDTPIM---NRYYNE---CfSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:PRK11658  311 EALKERGIGTGLHFRAAHTQKYYR------ERFPTLslpNTEWNSeriC-SLPLFPDMTDADVDRVITALQQIA 377
 
Name Accession Description Interval E-value
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
5-374 3.41e-164

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 464.49  E-value: 3.41e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   5 IPYGKQSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFV 83
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALgVGPGDRVWTTPITFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  84 ATSNSILYVEAIPIFVDIQ-EDGNIDLDLCEEELKKDSS--IKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLG 160
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDpDTGNIDEDALEKKLAAAKGklPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 161 ASFGNIKAGSCENSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKR------FPDTAPWYYEMHSLGFNY 234
Cdd:TIGR03588 161 AEYGGKPVGNCRYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKdpllfeKQDEGPWYYEQQELGFNY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 235 RITDMQVALGISQLKKLDSFIKRRKEIALKYDKAFL-NSFVKPLYSFTNN-SSYHLFVVKVDFsKLNISKIELFNKMREK 312
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKdLPYFTPLTIPLGSkSAWHLYPILLDQ-EFGCTRKEVFEALRAA 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054581693 313 NIGLQLHYIPINKQPYYKYlGYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-374 2.53e-152

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 433.73  E-value: 2.53e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   4 FIPYGKQSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSF 82
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALgIGPGDEVITPAFTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  83 VATSNSILYVEAIPIFVDIQED-GNIDLDLCEEELKKDssIKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGA 161
Cdd:COG0399    81 VATANAILYVGATPVFVDIDPDtYNIDPEALEAAITPR--TKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 162 SFGNIKAGSCenSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKRFPDtapwyYEMHSLGFNYRITDMQV 241
Cdd:COG0399   159 TYKGKKVGTF--GDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAK-----YEHVELGYNYRMDELQA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 242 ALGISQLKKLDSFIKRRKEIALKYDKAF--LNSFVKPLYSFTNNSSYHLFVVKVDfskLNISKIELFNKMREKNIGLQLH 319
Cdd:COG0399   232 AIGLAQLKRLDEFIARRRAIAARYREALadLPGLTLPKVPPGAEHVYHLYVIRLD---EGEDRDELIAALKARGIGTRVH 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054581693 320 Y-IPINKQPYYKYLGYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:COG0399   309 YpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
16-370 5.05e-131

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 379.19  E-value: 5.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  16 DINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFVATSNSILYVEA 94
Cdd:cd00616     1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALgIGPGDEVIVPSFTFVATANAILLLGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  95 IPIFVDIQED-GNIDLDLCEEELKKDssIKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGASFGNIKAGSCen 173
Cdd:cd00616    81 TPVFVDIDPDtYNIDPELIEAAITPR--TKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTF-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 174 SDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKRFpdtaPWYYEMHSLGFNYRITDMQVALGISQLKKLDS 253
Cdd:cd00616   157 GDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRD----RFKYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 254 FIKRRKEIALKYDKAFLN-SFVKPLYSFTNN-SSYHLFVVKVDfSKLNISKIELFNKMREKNIGLQLHYIPIN-KQPYYK 330
Cdd:cd00616   233 IIARRREIAERYKELLADlPGIRLPDVPPGVkHSYHLYVIRLD-PEAGESRDELIEALKEAGIETRVHYPPLHhQPPYKK 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1054581693 331 YLGYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTL 370
Cdd:cd00616   312 LLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
10-371 4.53e-118

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 346.58  E-value: 4.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  10 QSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFVATSNS 88
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALgVGPGDEVITPSFTFVATANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  89 ILYVEAIPIFVDIQ-EDGNIDLDLCEEELKKDSsiKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGASFGNIK 167
Cdd:pfam01041  81 ALRLGAKPVFVDIDpDTYNIDPEAIEAAITPRT--KAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 168 AGSCenSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIKRfPDTAPWYYEMhsLGFNYRITDMQVALGISQ 247
Cdd:pfam01041 159 VGTL--GDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVR-KADKRYWHEV--LGYNYRMTEIQAAIGLAQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 248 LKKLDSFIKRRKEIALKYDKAFL---NSFVKPLYSFTNNSSYHLFVVKVDFSKlnISKIELFNKMREKNIGLQLHY-IPI 323
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLAdlpGFTPLTTPPEADVHAWHLFPILVPEEA--INRDELVEALKEAGIGTRVHYpIPL 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1054581693 324 NKQPYYKYL-GYGNEDTPIMNRYYNECFSLPMYSSLSNEEQEYVIKTLF 371
Cdd:pfam01041 312 HLQPYYRDLfGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
1-374 4.05e-65

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 211.42  E-value: 4.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   1 MIDFIPYGKQSIDEDDINSVVEVLKSDFLTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTP 79
Cdd:PRK11658    1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALgIGPGDEVITPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  80 NSFVATSNSILYVEAIPIFVDIQEDG-NIDLDLCEEELKkdSSIKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHS 158
Cdd:PRK11658   81 LTWVSTLNMIVLLGATPVMVDVDRDTlMVTPEAIEAAIT--PRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 159 LGASFGNIKAGScenSDCSILSFHPVKHITTGEGGAVTTNSKEIYEKLLELRAHGIK----------RFPDTapwyyEMH 228
Cdd:PRK11658  159 VGTYYKGRHIGA---RGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGvdafdrqtqgRAPQA-----EVL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 229 SLGFNYRITDMQVALGISQLKKLDSFIKRRKEIALKYDKAFLNSFVKPLY--SFTNNSSYHLFVVKVDFSKLNISKIELF 306
Cdd:PRK11658  231 TPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSlpAWPHQHAWHLFIIRVDEERCGISRDALM 310
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054581693 307 NKMREKNIGLQLHYIPINKQPYYKylgygnEDTPIM---NRYYNE---CfSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:PRK11658  311 EALKERGIGTGLHFRAAHTQKYYR------ERFPTLslpNTEWNSeriC-SLPLFPDMTDADVDRVITALQQIA 377
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
3-376 1.19e-51

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 177.77  E-value: 1.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693   3 DFIPYGKQSIDEDDINSVVE-VLksDF-LTTGPKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVL---------LNK 71
Cdd:PRK15407   33 SPIPPSGKVIDAKELQNLVDaSL--DFwLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALtspklgdraLKP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  72 GDKVITTPNSFVATSNSILYVEAIPIFVDIQ-EDGNIDLDLCEEELKkdSSIKALYVVNFSGNIVNQKKLKYLKESYNIK 150
Cdd:PRK15407  111 GDEVITVAAGFPTTVNPIIQNGLVPVFVDVElPTYNIDASLLEAAVS--PKTKAIMIAHTLGNPFDLAAVKAFCDKHNLW 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 151 ILEDCAHSLGASFGNIKAGSCenSDCSILSFHPVKHITTGEGGAVTTNSKEIYeKLLE-LR--------AHGI-----KR 216
Cdd:PRK15407  189 LIEDNCDALGSTYDGRMTGTF--GDIATLSFYPAHHITMGEGGAVFTNDPLLK-KIIEsFRdwgrdcwcAPGCdntcgKR 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 217 FP---DTAPWYYEmHS-----LGFNYRITDMQVALGISQLKKLDSFIKRRKEiALKYDKAFLNSFVKPLY--SFTNNS-- 284
Cdd:PRK15407  266 FGwqlGELPFGYD-HKytyshLGYNLKITDMQAAIGLAQLEKLPGFIEARKA-NFAYLKEGLASLEDFLIlpEATPNSdp 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 285 SYHLFVVKVDfSKLNISKIELFNKMREKNIGLQLHYI-PINKQPYYKYLGY------GNEDTpIMNRyyneCFSLPMYSS 357
Cdd:PRK15407  344 SWFGFPITVK-EDAGFTRVELVKYLEENKIGTRLLFAgNLTRQPYFKGVKYrvvgelTNTDR-IMND----TFWIGVYPG 417
                         410
                  ....*....|....*....
gi 1054581693 358 LSNEEQEYVIKTLFEVLNV 376
Cdd:PRK15407  418 LTEEMLDYVIEKIEEFFGL 436
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
44-374 5.07e-34

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 129.18  E-value: 5.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  44 KYTNAKYCVAVANGTAALHLASLVL-LNKGDKVITTPNSFVATSNSILYVEAIPIFVDIQED-GNIDLDLCEEELKKDSs 121
Cdd:PRK11706   42 QRFGSAKVLLTPSCTAALEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDtMNIDETLIEAAITPKT- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 122 iKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGASFGNIKAGSCENSDCsiLSFHPVKHITTGEGGAVTTNSke 201
Cdd:PRK11706  121 -RAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGC--FSFHETKNYTAGEGGALLIND-- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 202 iyEKLLElRAHGIK-------RF----PDTAPWyyemHSLGFNYRITDMQVALGISQLKKLDSFIKRRKEIALKYDKAFL 270
Cdd:PRK11706  196 --PALIE-RAEIIRekgtnrsQFfrgqVDKYTW----VDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALA 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 271 -----NSFVKPLYSFTNNSSYHLFVVKVdfsKLNISKIELFNKMREKNIGLQLHYIPINKQPYYKYLGYGNEDTPIMNRY 345
Cdd:PRK11706  269 plaeaGRIELPSIPDDCKHNAHMFYIKL---RDLEDRSALINFLKEAGIMAVFHYIPLHSSPAGERFGRFHGEDRYTTKE 345
                         330       340
                  ....*....|....*....|....*....
gi 1054581693 346 YNECFSLPMYSSLSNEEQEYVIKTLFEVL 374
Cdd:PRK11706  346 SERLLRLPLFYNLTDVEQRTVIDTILEFF 374
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
35-154 8.88e-12

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 65.44  E-value: 8.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  35 IKEFEDELCKYTNAKY-------CVAVANG-TAALHLASLVLLNKGDKVITTPNSFVATSNSILYVEAIPIFVDIQEDGN 106
Cdd:cd00609    38 LPELREAIAEWLGRRGgvdvppeEIVVTNGaQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGG 117
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054581693 107 IDLDLCEEELKKDSSIKALYVVNFS---GNIVNQKKLKYLKE---SYNIKILED 154
Cdd:cd00609   118 FLLDLELLEAAKTPKTKLLYLNNPNnptGAVLSEEELEELAElakKHGILIISD 171
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
34-198 8.90e-09

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 54.31  E-value: 8.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  34 KIKEFEDELCKYTN--AKYCVAVANGTAALHLASLVLLNKGDKVITTPNSFVATSNSIL---YVEAIPIFVDIQEDGNID 108
Cdd:cd01494     1 KLEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAelaGAKPVPVPVDDAGYGGLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693 109 LDLCEEELKKD--SSIKALYVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLGASFGNIKAGSCENSDCSILSFHpvKH 186
Cdd:cd01494    81 VAILEELKAKPnvALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLH--KN 158
                         170
                  ....*....|..
gi 1054581693 187 ITTGEGGAVTTN 198
Cdd:cd01494   159 LGGEGGGVVIVK 170
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
35-129 1.88e-05

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 46.28  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  35 IKEFEDELCKYTNAKY-------CVAVANG-TAALHLASLVLLNKGDKVI-TTPnSFVATSNSILYVEAIPIFVDIQEDG 105
Cdd:COG0436    69 IPELREAIAAYYKRRYgvdldpdEILVTNGaKEALALALLALLNPGDEVLvPDP-GYPSYRAAVRLAGGKPVPVPLDEEN 147
                          90       100
                  ....*....|....*....|....*.
gi 1054581693 106 N--IDLDLCEEELKKDssIKALYVVN 129
Cdd:COG0436   148 GflPDPEALEAAITPR--TKAIVLNS 171
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
16-170 5.36e-05

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 44.55  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  16 DINSVVEvLKSDFLTTGPkIKEFEDELCKYTNAKYCVAVANGTAALHLAS-LVLLNKGDKVITTPNSFVATSNSILYVEA 94
Cdd:cd00615    44 DVTELTG-LDDLLDPTGP-IKEAQELAARAFGAKHTFFLVNGTSSSNKAViLAVCGPGDKILIDRNCHKSVINGLVLSGA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  95 IPIFVDIQED------GNIDLDLCEEELKKDSSIKALYVVN--FSGNIVNQKKLKYLKESYNIKILEDCAHSLGASFGNI 166
Cdd:cd00615   122 VPVYLKPERNpyygiaGGIPPETFKKALIEHPDAKAAVITNptYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPI 201

                  ....
gi 1054581693 167 KAGS 170
Cdd:cd00615   202 LPSS 205
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
37-165 1.71e-04

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 42.97  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  37 EFEDELCKYTNAKYCVAVANGTAALHLASLVLLNKGDKVITTPNS---FVATSNSILYVEAIPIFVDIQEDGNIDLDLCE 113
Cdd:pfam01212  36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAhihFDETGGHAELGGVQPRPLDGDEAGNMDLEDLE 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054581693 114 EELKKDSS-----IKALYVVN----FSGNIVNQKKLKYLKE---SYNIKILEDcahslGASFGN 165
Cdd:pfam01212 116 AAIREVGAdifppTGLISLENthnsAGGQVVSLENLREIAAlarEHGIPVHLD-----GARFAN 174
PRK09275 PRK09275
bifunctional aspartate transaminase/aspartate 4-decarboxylase;
53-145 2.11e-04

bifunctional aspartate transaminase/aspartate 4-decarboxylase;


Pssm-ID: 236444  Cd Length: 527  Bit Score: 43.32  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  53 AVANGTAALH--LASLV---LLNKGDKV-----ITTPnsfvatsnsilYVEaIPIF-------VDIQEDGNIDLDLCEEE 115
Cdd:PRK09275  166 AVEGGTAAMCyiFDSLKengLLKAGDKIalmtpIFTP-----------YLE-IPELprydlevVHINADEENEWQYPDSE 233
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1054581693 116 LKK--DSSIKALYVVNFS---GNIVNQKKLKYLKE 145
Cdd:PRK09275  234 LEKlrDPSIKALFLVNPSnppSVAMSDESLEKIAD 268
PRK08361 PRK08361
aspartate aminotransferase; Provisional
35-154 1.99e-03

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 39.86  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  35 IKEFEDELCKYTNAKYCVAV--------ANGTAALHLASLVLLNKGDKVITTPNSFVATSNSILYVEAIPIFVDIQEDGN 106
Cdd:PRK08361   72 IPELREAIAEYYKKFYGVDVdvdnvivtAGAYEATYLAFESLLEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENE 151
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054581693 107 IDLD---LCEEELKKDSSIKALYVVNFSGNIVNQKKLKY---LKESYNIKILED 154
Cdd:PRK08361  152 FQPDpdeLLELITKRTRMIVINYPNNPTGATLDKEVAKAiadIAEDYNIYILSD 205
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
33-85 2.20e-03

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 39.88  E-value: 2.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054581693  33 PKIKEFEDELCKYTNAKYCVAVANGTAALHLASLVLLNKGDKVITTPNSFVAT 85
Cdd:cd00614    40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASDDLYGGT 92
PRK05764 PRK05764
aspartate aminotransferase; Provisional
52-154 3.33e-03

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 39.34  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  52 VAVANGTA-ALHLASLVLLNKGDKV-ITTPnSFVATSNSILYVEAIPIFVDIQEDGNIDLDLceEELKK--DSSIKALyV 127
Cdd:PRK05764   94 VIVTTGAKqALYNAFMALLDPGDEViIPAP-YWVSYPEMVKLAGGVPVFVPTGEENGFKLTV--EQLEAaiTPKTKAL-I 169
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1054581693 128 VNF----SGNIVNQKKLKYLKE---SYNIKILED 154
Cdd:PRK05764  170 LNSpsnpTGAVYSPEELEAIADvavEHDIWVLSD 203
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
51-160 5.00e-03

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 38.58  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054581693  51 CVAVANGTAALHLA--SLVLLNKGDKVITT----PNSFVATSNSILYVEAIPIFVDIQEDGNIDLDLCEEELKKDSSIKA 124
Cdd:COG0520    80 IIFTRGTTEAINLVayGLGRLKPGDEILITemehHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVA 159
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1054581693 125 L-YVVNFSGNIVNQKKLKYLKESYNIKILEDCAHSLG 160
Cdd:COG0520   160 VtHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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